(data stored in ACNUC7421 zone)

SWISSPROT: PTH_ANADF

ID   PTH_ANADF               Reviewed;         192 AA.
AC   A7H6J5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   11-DEC-2019, entry version 68.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=Anae109_0123;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acyl-L-alpha-aminoacyl-tRNA = an N-acyl-L-amino acid +
CC         H(+) + tRNA; Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59874,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:138191; EC=3.1.1.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00083};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
DR   EMBL; CP000769; ABS24341.1; -; Genomic_DNA.
DR   RefSeq; WP_011984447.1; NC_009675.1.
DR   STRING; 404589.Anae109_0123; -.
DR   EnsemblBacteria; ABS24341; ABS24341; Anae109_0123.
DR   KEGG; afw:Anae109_0123; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   OrthoDB; 1676462at2; -.
DR   BioCyc; ASP404589:G1G9J-127-MONOMER; -.
DR   Proteomes; UP000006382; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
DR   Gene3D; 3.40.50.1470; -; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A7H6J5.
DR   SWISS-2DPAGE; A7H6J5.
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..192
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000010558"
SQ   SEQUENCE   192 AA;  20711 MW;  E6BE2F8BF170D622 CRC64;
     MKLVVGLGNP GPEYARTRHN VGFLVADRLA LALRAEFTLR KFASELAEGR AGGERVWIMK
     PQTYMNHSGE SVGSALHFWK LGLEDLVVVH DDLELEPFRV QLKVGGGHGG HNGLKSVNAH
     VGGPDYARVR VGVGRPPPRM DPADYVLGRF AKADEAPLEE CLVRATEAAR LAIELGAAKA
     MNQVNRRASA AG
//

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